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Literature DB >> 18763771

Comparison of "Polarization inversion with spin exchange at magic angle" and "geometric analysis of labeled alanines" methods for transmembrane helix alignment.

Vitaly V Vostrikov¹, Christopher V Grant, Anna E Daily, Stanley J Opella, Roger E Koeppe.

Abstract

Using the model alpha-helical peptide acetyl-GGALW5LALALALALALALW19LAGA-ethanolamide ("GWALP23"), we have compared the polarization inversion with spin exchange at magic angle method and geometric analysis of labeled alanines method for estimating the transmembrane helix orientation. For GWALP23 in bilayers of a short lipid, dilauroylphosphatidylcholine, we find general agreement between the two methods, with a static helix tilt of about 11degrees-13degrees with respect to the bilayer normal.

Entities: Chemical Disease Gene

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Year: 2008 PMID： 18763771 PMCID： PMC2609751 DOI： 10.1021/ja803734k

Source DB: PubMed Journal: J Am Chem Soc ISSN： 0002-7863 Impact factor: 15.419

17 in total

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3. Structural features of transmembrane helices.

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6. Different membrane anchoring positions of tryptophan and lysine in synthetic transmembrane alpha-helical peptides.

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7. Geometry and intrinsic tilt of a tryptophan-anchored transmembrane alpha-helix determined by (2)H NMR.

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8. Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane alpha-helical peptides: importance of hydrophobic mismatch and proposed role of tryptophans.

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9. Tilt angles of transmembrane model peptides in oriented and non-oriented lipid bilayers as determined by 2H solid-state NMR.

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10. Electrospray ionization mass spectrometry as a tool to analyze hydrogen/deuterium exchange kinetics of transmembrane peptides in lipid bilayers.

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30 in total

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